Ontology highlight
ABSTRACT:
SUBMITTER: Du X
PROVIDER: S-EPMC3843099 | biostudies-literature | 2013 Nov
REPOSITORIES: biostudies-literature
Du Xin X Chen Nelson L H NL Wong Andre A Craik Charles S CS Brömme Dieter D
The Journal of biological chemistry 20131011 48
Cathepsin V is a highly effective elastase and has been implicated in physiological and pathological extracellular matrix degradation. However, its mechanism of action remains elusive. Whereas human cathepsin V exhibits a potent elastolytic activity, the structurally homologous cathepsin L, which shares a 78% amino acid sequence, has only a minimal proteolytic activity toward insoluble elastin. This suggests that there are distinct structural domains that play an important role in elastinolysis. ...[more]